Light‐Induced Mechanistic Divergence in Gold(I) Catalysis: Revisiting the Reactivity of Diazonium Salts

In a systematic study of the Au‐catalyzed reaction of o‐alkynylphenols with aryldiazonium salts, we find that essentially the same reaction conditions lead to a change in mechanism when a light source is applied. If the reaction is carried out at room temperature using a Au^I catalyst, the diazonium salt undergoes electrophilic deauration of a vinyl Au^I intermediate and provides access to substituted azobenzofurans. If the reaction mixture is irradiated with blue LED light, C?C bond formation due to N₂‐extrusion from the diazonium salt is realized selectively, using the same starting materials without the need for an additional photo(redox) catalyst under aerobic conditions. We report a series of experiments demonstrating that the same vinyl Au^I intermediate is capable of producing the observed products under photolytic and thermal conditions. The finding that a vinyl Au^I complex can directly, without the need for an additional photo(redox) catalyst, result in C?C bond formation under photolytic conditions is contrary to the proposed mechanistic pathways suggested in the literature till date and highlights that the role of oxidation state changes in photoredox catalysis involving Au is thus far only poorly understood and may hold surprises for the future. Computational results indicate that photochemical activation can occur directly from a donor–acceptor complex formed between the vinyl Au^I intermediate and the diazonium salt.     

Micellar Catalysis for Ruthenium(II)‐Catalyzed C−H Arylation: Weak‐Coordination‐Enabled C−H Activation in H2O

Chemoselective C?H arylations were accomplished through micellar catalysis by a versatile single‐component ruthenium catalyst. The strategy provided expedient access to C?H‐arylated ferrocenes with wide functional‐group tolerance and ample scope through weak chelation assistance. The sustainability of the C?H arylation was demonstrated by outstanding atom‐economy and recycling studies. Detailed computational studies provided support for a facile C?H activation through thioketone assistance.     

Immunological Analysis of Isothiocyanate-Modified α-Lactalbumin Using High-Performance Thin Layer Chromatography

Undirected modifications between food proteins and secondary plant metabolites can occur during food processing. The results of covalent interactions can alter the functional and biological properties of the proteins. The present work studied the extent of which covalent conjugation of the bioactive metabolite benzyl isothiocyanate (BITC; a glucosinolate breakdown product) to the whey protein α-lactalbumin affects the protein’s allergenicity. Additional to the immunological analysis of native untreated and BITC-modified α-lactalbumin, the analysis of antigenic properties of proteolytically digested protein derivatives was also performed by high performance thin layer chromatography and immunostaining. As a result of the chemical modifications, structural changes in the protein molecule affected the allergenic properties. In this process, epitopes are destroyed or inactivated, but at the same time, buried epitopes can be exposed or newly formed, so that the net effect was an increase in allergenicity, in this case. Results from the tryptic hydrolysis suggest that BITC conjugation sterically hindered the cleavage sites for the enzyme, resulting in reduced digestibility and allergenicity. Residual antigenicity can be still present as short peptide fragments that provide epitopes. The desire to make food safer for allergy sufferers and to protect sensitized individuals from an allergenic reaction makes it clear that the detection of food antigens is mandatory; especially by considering protein interactions.     

Geometric E→Z Isomerisation of Alkenyl Silanes by Selective Energy Transfer Catalysis: Stereodivergent Synthesis of Triarylethylenes via a Formal anti‐Metallometallation

An efficient geometrical E→Z isomerisation of alkenyl silanes is disclosed via selective energy transfer using an inexpensive organic sensitiser. Characterised by operational simplicity, short reaction times (2 h), and broad substrate tolerance, the reaction displays high selectivity for trisubstituted systems (Z/E up to 95:5). In contrast to thermal activation, directionality results from deconjugation of the π‐system in the Z‐isomer due to A^1,3‐strain thereby inhibiting re‐activation. The structural importance of the β‐substituent logically prompted an investigation of mixed bis‐nucleophiles (Si, Sn, B). These versatile linchpins also undergo facile isomerisation, thereby enabling a formal anti‐metallometallation. Mechanistic interrogation, supported by a theoretical investigation, is disclosed together with application of the products to the stereospecific synthesis of biologically relevant target structures.     

Hydrogenation of Esters to Alcohols with a Well‐Defined Iron Complex

We present the first base‐free Fe‐catalyzed ester reduction applying molecular hydrogen. Without any additives, a variety of carboxylic acid esters and lactones were hydrogenated with high efficiency. Computations reveal an outer‐sphere mechanism involving simultaneous hydrogen transfer from the iron center and the ligand. This assumption is supported by NMR experiments.     

Ultra‐Low‐Field NMR Relaxation and Diffusion Measurements Using an Optical Magnetometer

Nuclear magnetic resonance (NMR) relaxometry and diffusometry are important tools for the characterization of heterogeneous materials and porous media, with applications including medical imaging, food characterization and oil‐well logging. These methods can be extremely effective in applications where high‐resolution NMR is either unnecessary, impractical, or both, as is the case in the emerging field of portable chemical characterization. Here, we present a proof‐of‐concept experiment demonstrating the use of high‐sensitivity optical magnetometers as detectors for ultra‐low‐field NMR relaxation and diffusion measurements.     

Carbohydrate‐Based Nanocarriers Exhibiting Specific Cell Targeting with Minimum Influence from the Protein Corona

Whenever nanoparticles encounter biological fluids like blood, proteins adsorb on their surface and form a so‐called protein corona. Although its importance is widely accepted, information on the influence of surface functionalization of nanocarriers on the protein corona is still sparse, especially concerning how the functionalization of PEGylated nanocarriers with targeting agents will affect protein corona formation and how the protein corona may in turn influence the targeting effect. Herein, hydroxyethyl starch nanocarriers (HES‐NCs) were prepared, PEGylated, and modified on the outer PEG layer with mannose to target dendritic cells (DCs). Their interaction with human plasma was then studied. Low overall protein adsorption with a distinct protein pattern and high specific affinity for DC binding were observed, thus indicating an efficient combination of “stealth” and targeting behavior.